Recent work has indicated G-glucoronidation as a novel mammalian metabolic pathway. Since C-glucuronides are resistant to Beta-glucuronidase hydrolysis, they can not be identified by normal methods using this hydrolysis to regenerate the aglycone from the conjugate. This project is aimed at the examination of purified UDPG transferases to discover if the specific ability to conjugate at carbon is associated with different forms of UDPGT. At present the extent and degree of C-glucuronidation is not known as the enzymes carrying out this function have not been isolated. Since C-glucuronidation has been found to occur in phenolic structures and in some common drug molecules, this pathway is clearly of far greater general importance than has been realized heretofore, and has important implications in drug and xenobiotic detoxification mechanisms. Purified enzyme preparations will be examined for conjugating ability using the known substances found to give C-glucuronidation so far, and products will be isolated and characterized.